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2MAL

Solution structure of Lipid Transfer Protein from Lentil Lens Culinaris

2LJO」から置き換えられました
2MAL の概要
エントリーDOI10.2210/pdb2mal/pdb
関連するPDBエントリー1AFH 1BV2 1BWO 1CZ2 1GH1 1LIP 1RZL 1SIY 1T12 1UVA 1UVB 1UVC
NMR情報BMRB: 19365
分子名称Non-specific lipid-transfer protein 2 (1 entity in total)
機能のキーワードplant lipid transfer protein, lens culinaris, lipid transport
由来する生物種Lens culinaris (Lentil)
タンパク質・核酸の鎖数1
化学式量合計9299.69
構造登録者
Gizatullina, A.K.,Mineev, K.S.,Shenkarev, Z.O. (登録日: 2013-07-16, 公開日: 2013-10-02, 最終更新日: 2024-11-20)
主引用文献Gizatullina, A.K.,Finkina, E.I.,Mineev, K.S.,Melnikova, D.N.,Bogdanov, I.V.,Telezhinskaya, I.N.,Balandin, S.V.,Shenkarev, Z.O.,Arseniev, A.S.,Ovchinnikova, T.V.
Recombinant production and solution structure of lipid transfer protein from lentil Lens culinaris.
Biochem.Biophys.Res.Commun., 439:427-432, 2013
Cited by
PubMed Abstract: Lipid transfer protein, designated as Lc-LTP2, was isolated from seeds of the lentil Lens culinaris. The protein has molecular mass 9282.7Da, consists of 93 amino acid residues including 8 cysteines forming 4 disulfide bonds. Lc-LTP2 and its stable isotope labeled analogues were overexpressed in Escherichia coli and purified. Antimicrobial activity of the recombinant protein was examined, and its spatial structure was studied by NMR spectroscopy. The polypeptide chain of Lc-LTP2 forms four α-helices (Cys4-Leu18, Pro26-Ala37, Thr42-Ala56, Thr64-Lys73) and a long C-terminal tail without regular secondary structure. Side chains of the hydrophobic residues form a relatively large internal tunnel-like lipid-binding cavity (van der Waals volume comes up to ∼600Å(3)). The side-chains of Arg45, Pro79, and Tyr80 are located near an assumed mouth of the cavity. Titration with dimyristoyl phosphatidylglycerol (DMPG) revealed formation of the Lc-LTP2/lipid non-covalent complex accompanied by rearrangements in the protein spatial structure and expansion of the internal cavity. The resultant Lc-LTP2/DMPG complex demonstrates limited lifetime and dissociates within tens of hours.
PubMed: 23998937
DOI: 10.1016/j.bbrc.2013.08.078
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mal
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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